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Park, Chan Young
Calcium Dynamics Lab
Research Interests
  • Calcium Signaling, Calcium Channels, Immune, neuroscience, Drug Development, Virus and host cell interaction.

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AtCML8, a calmodulin-like protein, differentially activating CaM-dependent enzymes in Arabidopsis thaliana

Cited 7 times inthomson ciCited 6 times inthomson ci
Title
AtCML8, a calmodulin-like protein, differentially activating CaM-dependent enzymes in Arabidopsis thaliana
Author
Park, Hyeong CheolPark, Chan YoungKoo, Sung CheolCheong, Mi SunKim, Kyung EunKim, Min ChulLim, Chae OhLee, Sang YeolYun, Dae-JinChung, Woo Sik
Issue Date
2010-11
Publisher
SPRINGER
Citation
PLANT CELL REPORTS, v.29, no.11, pp.1297 - 1304
Abstract
Plants express many calmodulins (CaMs) and calmodulin-like (CML) proteins that sense and transduce different Ca(2+) signals. Previously, we reported divergent soybean (Glycine max) CaM isoforms (GmCaM4/5) with differential abilities to activate CaM-dependent enzymes. To elucidate biological functions of divergent CaM proteins, we isolated a cDNA encoding a CML protein, AtCML8, from Arabidopsis. AtCML8 shows highest identity with GmCaM4 at the protein sequence level. Expression of AtCML8 was high in roots, leaves, and flowers but low in stems. In addition, the expression of AtCML8 was induced by exposure to salicylic acid or NaCl. AtCML8 showed typical characteristics of CaM such as Ca(2+)-dependent electrophoretic mobility shift and Ca(2+) binding ability. In immunoblot analyses, AtCML8 was recognized only by antiserum against GmCaM4 but not by GmCaM1 antibodies. Interestingly, AtCML8 was able to activate phosphodiesterase (PDE) but did not activate NAD kinase. These results suggest that AtCML8 acts as a CML protein in Arabidopsis with characteristics similar to soybean divergent GmCaM4 at the biochemical levels.
URI
https://scholarworks.unist.ac.kr/handle/201301/10017
URL
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=77958482871
DOI
10.1007/s00299-010-0916-7
ISSN
0721-7714
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